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J. Biochem, 1988, Vol. 104, No. 4 537-543
© 1988 Japanese Biochemical Society

research-article

Amino Acid Sequence of Winged Bean (Psophocarpus tetragonolobus (L.) DC.) Chymotrypsin Inhibitor, WCI-31

Hiroshi Shibata, Saburo Hara2 and Tokuji Ikenaka

Department of Chemistry, Osaka University College of Science Toyonaka, Osaka 560

2To whom correspondence should be addressed

The complete amino acid sequence of winged bean chymotrypsin inhibitor 3 (WCI-3) was determined by the conventional methods. WCI-3 consisted of 183 amino acid residues, but was heterogeneous in the carboxyl terminal region owing to the loss of one to four carboxyl terminal amino acid residues. The sequence of WCI-3 was highly homologous with those of soybean trypsin inhibitor Tia, winged bean trypsin inhibitor WTI-1, and Erythrina latissima trypsin inhibitor DE-3. One of the reactive site peptide bonds of WCI-3 was identified as Leu(65)-Ser(66), which was located at the same position as those of the other Kunitz-family leguminous proteinase inhibitors.

1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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